Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6GQJ7

Entry ID Method Resolution Chain Position Source
AF-Q6GQJ7-F1 Predicted AlphaFoldDB

No variants for Q6GQJ7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6GQJ7

No associated diseases with Q6GQJ7

3 regional properties for Q6GQJ7

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 137 - 148 IPR001412
domain DALR anticodon binding 465 - 580 IPR008909
domain Arginyl-tRNA synthetase, catalytic core domain 126 - 451 IPR035684

Functions

Description
EC Number 6.1.1.19 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Mitochondrion membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

2 GO annotations of molecular function

Name Definition
arginine-tRNA ligase activity Catalysis of the reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

1 GO annotations of biological process

Name Definition
arginyl-tRNA aminoacylation The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. The arginyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of an alanine accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAWHFRRVIA EQVSRVLGLP SESCSRVAQC IQTVPVHRKH ESPDFQLFMT SLSEGGPNGT
70 80 90 100 110 120
FSNQEERAEQ LAGKLVCDSV ISDIGTTRGS VTFKINRDLL TRNVLQQISK DGSLYGLNTE
130 140 150 160 170 180
LFSELSRRKT IVEYSSPNIA KKFHVGHLRS TIIGNFIANL KQAVGNEVVR INYLGDWGLQ
190 200 210 220 230 240
FGLLGAGFSS FGSKEKLLAN PLQHLFEVYV KVNTAAEKDN GIKLSAQEFL RRLEGGDPHA
250 260 270 280 290 300
LSLWMHFRDI SIQEYAKIYK RLGAHFDDYS GESFYKEKSQ EVLKQLESKG LLLKTDKGTV
310 320 330 340 350 360
IDLSEEGNLS SYSTVMRSDG TSLYITRDMA AAVDRMERYN FDEMIYVTDK SQKNHFQQLF
370 380 390 400 410 420
KILKIMGKDQ ADRCQHVPFG LVQGMKTRRG EVVFLEDVLD EARSRMLQNM AASETSKQLD
430 440 450 460 470 480
DPSDTAEKIG IAALIVQDFK GQLVSDYHFD WDQALQSTGD TGVFLQYTHA RLHSLQALRC
490 500 510 520 530 540
PRDTEDFEIA SLREPCVIAT LQHLLRYDEV IYKCLEDLQP RYLVTYLLSL GHLANVAHRT
550 560 570
LQVKGSSSEA AHARLLFFKN VQMVLGNGMK LLGITPVNNM